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• W2111713855 abstract "The prokaryotic V-ATPase of Enterococcus hirae , closely related to the eukaryotic enzymes, provides a unique opportunity to study the ion-translocation mechanism because it transports Na + , which can be detected by radioisotope ( ) experiments and X-ray crystallography. In this study, we demonstrated that the binding affinity of the rotor ring (K ring) for decreased approximately 30-fold by reaction with N , N ′ -dicyclohexylcarbodiimide (DCCD), and determined the crystal structures of Na + -bound and Na + -unbound K rings modified with DCCD at 2.4- and 3.1-Å resolutions, respectively. Overall these structures were similar, indicating that there is no global conformational change associated with release of Na + from the DCCD-K ring. A conserved glutamate residue (E139) within all 10 ion-binding pockets of the K ring was neutralized by modification with DCCD, and formed an “open” conformation by losing hydrogen bonds with the Y68 and T64 side chains, resulting in low affinity for Na + . This open conformation is likely to be comparable to that of neutralized E139 forming a salt bridge with the conserved arginine of the stator during the ion-translocation process. Based on these findings, we proposed the ion-translocation model that the binding affinity for Na + decreases due to the neutralization of E139, thus releasing bound Na + , and that the structures of Na + -bound and Na + -unbound DCCD-K rings are corresponding to intermediate states before and after release of Na + during rotational catalysis of V-ATPase, respectively." @default.
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• W2111713855 date "2011-08-03" @default.
• W2111713855 modified "2023-10-03" @default.
• W2111713855 title "Structure of the rotor ring modified with <i>N</i> , <i>N</i> ^′ -dicyclohexylcarbodiimide of the Na ⁺ -transporting vacuolar ATPase" @default.
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• W2111713855 doi "https://doi.org/10.1073/pnas.1103287108" @default.
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